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Biochem J. 2018 May 24;475(10):1739-1753. doi: 10.1042/BCJ20170935.

The functional principle of eukaryotic molybdenum insertases.

Author information

1
Department of Plant Biology, Braunschweig University of Technology, 38106 Braunschweig, Germany.
2
Department of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, NM 87131-0001, U.S.A.
3
Structure and Function of Proteins, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.
4
Department for Biotechnology, Institute of Biochemistry, Biotechnology and Bioinformatics, Braunschweig University of Technology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
5
Department of Plant Biology, Braunschweig University of Technology, 38106 Braunschweig, Germany t.kruse@tu-bs.de.

Abstract

The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco biosynthesis involves several enzymes that catalyze the subsequent conversion of GTP into cyclic pyranopterin monophosphate (cPMP), molybdopterin (MPT), adenylated MPT (MPT-AMP), and finally Moco. While the underlying principles of cPMP, MPT, and MPT-AMP formation are well understood, the molybdenum insertase (Mo-insertase)-catalyzed final Moco maturation step is not. In the present study, we analyzed high-resolution X-ray datasets of the plant Mo-insertase Cnx1E that revealed two molybdate-binding sites within the active site, hence improving the current view on Cnx1E functionality. The presence of molybdate anions in either of these sites is tied to a distinctive backbone conformation, which we suggest to be essential for Mo-insertase molybdate selectivity and insertion efficiency.

KEYWORDS:

Mo-insertase; molybdenum cofactor maturation; molybdenum cofactor synthesis

PMID:
29717023
PMCID:
PMC6639804
DOI:
10.1042/BCJ20170935
[Indexed for MEDLINE]
Free PMC Article

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